Final answer:
Hydrophobic amino acids like valine, leucine, and isoleucine have nonpolar uncharged R groups which contribute to their hydrophobic nature.
Step-by-step explanation:
All hydrophobic amino acids, such as valine, leucine, isoleucine, and others, share the common property of having nonpolar uncharged R groups. These side chains do not have an affinity for water, which makes them hydrophobic or water-fearing. The characteristics of the side chains, which can be nonpolar, polar, acidic, or basic, greatly influence the structure and function of proteins. In the case of hydrophobic amino acids, their aliphatic or aromatic side chains foster hydrophobic interactions within proteins, affecting their configuration and interactions with other molecules.